Difference between revisions of "Phosphoserine amino-transferase"

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(Parameters with uncertainty)
(Parameters with uncertainty)
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* serC is the enzyme concentration collected from Turnaev ''et. al.'' <ref name="Turnaev_2006"></ref> which is considered to be fixed.
 
* serC is the enzyme concentration collected from Turnaev ''et. al.'' <ref name="Turnaev_2006"></ref> which is considered to be fixed.
 
* Mean and standard deviation for <math>Kc_{PHP}</math> and <math>Kc_{PSER}</math> is reported in <ref name="Ali_2006">Ali, V., and T. Nozaki, (2006), ''Biochemical and functional characterization of phosphoserine aminotransferase from Entamoeba histolytica, which possesses both phosphorylated and non-phosphorylated serine metabolic pathways'', Mol. Biochem. Parasitol. 145:71-83</ref> for ''Entamoeba histolytica''(an anaerobic parasitic protozoan). The values are <math>Kc_{PHP} = 0.058 \pm 0.021 </math> and <math>Kc_{PSER} = 0.0368 \pm 0.004 </math>
 
* Mean and standard deviation for <math>Kc_{PHP}</math> and <math>Kc_{PSER}</math> is reported in <ref name="Ali_2006">Ali, V., and T. Nozaki, (2006), ''Biochemical and functional characterization of phosphoserine aminotransferase from Entamoeba histolytica, which possesses both phosphorylated and non-phosphorylated serine metabolic pathways'', Mol. Biochem. Parasitol. 145:71-83</ref> for ''Entamoeba histolytica''(an anaerobic parasitic protozoan). The values are <math>Kc_{PHP} = 0.058 \pm 0.021 </math> and <math>Kc_{PSER} = 0.0368 \pm 0.004 </math>
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*For the turnover number (<math>KcatC</math>)10% Std. Dev. is considered.
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{|class="wikitable"
 
{|class="wikitable"
 
! Parameter
 
! Parameter
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|<math>KcatC</math>
 
|<math>KcatC</math>
|1.75 <ref name="drewke_1996">Drewke C, Klein M, Clade D et al (1996) 4-O-phosphoryl-L-threonine, a substrate of the pdxC(serC) gene product involved in vitamin B6 biosynthesis. FEBS Lett 390:179–182 </ref>
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|<math>1.75 \pm 0.175 </math>
 
|1/s
 
|1/s
 
|-
 
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Revision as of 17:18, 6 May 2014


This enzyme catalyzes reaction to convert Phosphohydroxypyruvate (PHP) to phosphoserine (PSER).

Chemical equation

PHP \rightleftharpoons PSER

Rate equation

Special rate equation [1] is used.

 \frac{serC * KcatC * \frac{[PHP]}{Kc_{PHP}} }{ 1 + \frac{[PHP]}{Kc_{PHP}} + \frac{[PSER]}{Kc_{PSER}} }

Parameter values

Parameter Value Units Organism Remarks
serC 0.1 [2] mM Escherichia coli
KcatC 1.75 [3] 1/s
Kc_{PHP} 0.0015[3] mM
Kc_{PSER} 0.0017[3] mM


Parameters with uncertainty

  • serC is the enzyme concentration collected from Turnaev et. al. [2] which is considered to be fixed.
  • Mean and standard deviation for Kc_{PHP} and Kc_{PSER} is reported in [4] for Entamoeba histolytica(an anaerobic parasitic protozoan). The values are Kc_{PHP} = 0.058 \pm 0.021 and Kc_{PSER} = 0.0368 \pm 0.004
  • For the turnover number (KcatC)10% Std. Dev. is considered.
Parameter Value Units Organism Remarks
serC 0.1 [2] mM Escherichia coli
KcatC 1.75 \pm 0.175 1/s
Kc_{PHP} 0.058 \pm 0.021 mM Entamoeba histolytica
Kc_{PSER} 0.0368 \pm 0.004 mM Entamoeba histolytica

References

  1. Smallbone K, Stanford NJ (2013). Kinetic modeling of metabolic pathways: Application to serine biosynthesis. In: Systems Metabolic Engineering, Humana Press. pp. 113–121
  2. 2.0 2.1 2.2 Turnaev II, Ibragimova SS, Usuda Y et al (2006). Mathematical modeling of serine and glycine synthesis regulation in Escherichia coli. Proceedings of the fifth international conference on bioinformatics of genome regulation and structure 2:78–83
  3. 3.0 3.1 3.2 Drewke C, Klein M, Clade D et al (1996) 4-O-phosphoryl-L-threonine, a substrate of the pdxC(serC) gene product involved in vitamin B6 biosynthesis. FEBS Lett 390:179–182
  4. Ali, V., and T. Nozaki, (2006), Biochemical and functional characterization of phosphoserine aminotransferase from Entamoeba histolytica, which possesses both phosphorylated and non-phosphorylated serine metabolic pathways, Mol. Biochem. Parasitol. 145:71-83